Selective and quantitative photochemical conversion of the tryptophyl residues to kynurenine in lysozyme
- 1 April 1968
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 31 (2) , 158-163
- https://doi.org/10.1016/0006-291x(68)90723-7
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- Dye-sensitized selective photooxidation of methioxineBiochimica et Biophysica Acta (BBA) - Protein Structure, 1968
- PROFLAVINE‐SENSITIZED PHOTOOXIDATION OF TRYPTOPHAN AND RELATED PEPTIDESPhotochemistry and Photobiology, 1967
- Non-enzymatic cleavage of tryptophyl peptide bonds in peptides and proteins: II. Release of a chemically modified tryptophan residue from model peptides by a mild basic treatmentBiochimica et Biophysica Acta (BBA) - General Subjects, 1966
- Studies on Polypeptides. XXXIV. Enzymic Properties of Partially Synthetic De(16-20)- and De(15-20)-ribonucleases S'1-3Journal of the American Chemical Society, 1966
- Action of sulfite on lysozymeArchives of Biochemistry and Biophysics, 1966
- Inattivazione della gramicidina dovuta alla conversione triptofano → N'-FormilchinureninaCellular and Molecular Life Sciences, 1964
- A Study of Factors Influencing the Reactivation of Reduced Egg White LysozymeJournal of Biological Chemistry, 1963
- The reductive cleavage of disulfide bonds and its application to problems of protein structureBiochimica et Biophysica Acta, 1959
- THE DETERMINATION OF LYSOZYMEJournal of Bacteriology, 1949